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Glutathione and detoxification
Cancer Treatment Reviews, 1990Cisplatin is recognized as one of the most effective drugs in the treatment of a variety of solid tumors. Its therapeutic usefulness has been limited by acute and cumulative nephrotoxicity ( 13). This side-effect is dose-dependent and requires adequate protective measures.
Saro Oriana +6 more
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Regulatory phenomena in the glutathione peroxidase superfamily.
Antioxidants and Redox Signaling, 2019Expression of glutathione peroxidases (GPxs) and the regulatory consequences of their action are reviewed. The selenium-containing GPXs 1-4 protect against oxidative challenge, inhibit inflammation and oxidant-induced regulated cell death.
R. Brigelius-Flohé, L. Flohé
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Detoxication reactions of glutathione and glutathione transferases
Xenobiotica, 1986(1986). Detoxication reactions of glutathione and glutathione transferases. Xenobiotica: Vol. 16, No. 10-11, pp. 957-973.
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The glutathione peroxidase activity of glutathione S-transferases
Biochimica et Biophysica Acta (BBA) - Enzymology, 1980Glutatione transferases (RX:glutathione R-transferases, EC 2.5.1.18) B and AA were purified from rat liver to investigate the mechanism for their apparent GSH peroxidase activity (GSSG formation). Both transferases catalyze an overall reaction in which loss of cumene hydroperoxide is accompanied by a stoichiometric increase in GSSG.
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Current Opinion in Clinical Nutrition and Metabolic Care, 2001
Altered glutathione metabolism in association with increased oxidative stress has been implicated in the pathogenesis of many diseases. However, whether strategies aimed at restoring glutathione concentration and homeostasis are effective in ameliorating or modifying the natural history of these states is unknown.
Marvin Reid, Farook Jahoor
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Altered glutathione metabolism in association with increased oxidative stress has been implicated in the pathogenesis of many diseases. However, whether strategies aimed at restoring glutathione concentration and homeostasis are effective in ameliorating or modifying the natural history of these states is unknown.
Marvin Reid, Farook Jahoor
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Glutathione Peroxidase and Glutathione Reductase Activities toward Glutathione-Derived Antioxidants
Biochemical and Biophysical Research Communications, 1994A new class of glutathione derivatives with antioxidant properties has been prepared by transformation of the NH2 group into a pyrrole ring with various substitutions at the 2 and 5 positions. Due to steric hindrance and/or hydrophobicity of the 2-5-disubstituted pyrrole ring, the reduced glutathione derivatives are poor substrates of the glutathione ...
P. Lafontant +5 more
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1996
Glutathione (GSH), the most ubiquitous and abundant nonprotein thiol, is essential in numerous detoxification reactions and is therefore considered a chemoprotectant. In the human, levels of GSH range from 30μM in plasma to 3mM in kidney proximal tubules; tumors of various organs can contain up to 10mM GSH [1].
Abhijit Raha, Kenneth D. Tew
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Glutathione (GSH), the most ubiquitous and abundant nonprotein thiol, is essential in numerous detoxification reactions and is therefore considered a chemoprotectant. In the human, levels of GSH range from 30μM in plasma to 3mM in kidney proximal tubules; tumors of various organs can contain up to 10mM GSH [1].
Abhijit Raha, Kenneth D. Tew
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Annual Review of Pharmacology and Toxicology, 2005
▪ Abstract This review describes the three mammalian glutathione transferase (GST) families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated MAPEG. Besides detoxifying electrophilic xenobiotics, such as chemical carcinogens, environmental pollutants, and antitumor agents, these transferases inactivate endogenous α,β ...
Hayes, John D. +2 more
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▪ Abstract This review describes the three mammalian glutathione transferase (GST) families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated MAPEG. Besides detoxifying electrophilic xenobiotics, such as chemical carcinogens, environmental pollutants, and antitumor agents, these transferases inactivate endogenous α,β ...
Hayes, John D. +2 more
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Biochemistry (Moscow), 2007
Many functions of mitochondrial GSH are significantly different from those of cytosolic GSH. This review considers the peculiarity of functions of mitochondrial GSH and enzymes of its metabolism, especially glutathione peroxidase 4, glutaredoxin 2, and kappa-glutathione transferase.
L. S. Kolesnichenko, V. I. Kulinsky
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Many functions of mitochondrial GSH are significantly different from those of cytosolic GSH. This review considers the peculiarity of functions of mitochondrial GSH and enzymes of its metabolism, especially glutathione peroxidase 4, glutaredoxin 2, and kappa-glutathione transferase.
L. S. Kolesnichenko, V. I. Kulinsky
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